Active site structure and redox processes of cytochrome c oxidase immobilised in a novel biomimetic lipid membrane on an electrode

Membrane-bound cytochrome c oxidase was attached to an electrode via a His-tag linker and studied by surface enhanced resonance Raman spectroscopy, demonstrating intact redox site structures and electron transfer between the electrode and the immobilized enzyme.

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2004-11 (21), p.2376-2377
Main Authors: Friedrich, Marcel G, Giebeta, Frank, Naumann, Renate, Knoll, Wolfgang, Ataka, Kenichi, Heberle, Joachim, Hrabakova, Jana, Murgida, Daniel H, Hildebrandt, Peter
Format: Article
Language:English
Subjects:
Binding Sites
Biomimetic Materials - chemistry
Electrodes
Electron Transport Complex IV - chemistry
Enzymes, Immobilized - chemistry
Membrane Lipids - chemistry
Oxidation-Reduction
Protein Conformation
Protein Structure, Tertiary
Rhodobacter sphaeroides - enzymology
Silver - chemistry
Surface Properties
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Description
Summary:Membrane-bound cytochrome c oxidase was attached to an electrode via a His-tag linker and studied by surface enhanced resonance Raman spectroscopy, demonstrating intact redox site structures and electron transfer between the electrode and the immobilized enzyme.
ISSN:1359-7345
1364-548X
DOI:10.1039/b410998h